IIB   20738
INSTITUTO DE INVESTIGACIONES BIOLOGICAS
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
STRUCTURAL FEATURES OF StAsp-PSIr AND SAPLIPs COULD EXPLAIN CYTOTOXIC SELECTIVITY
Autor/es:
MUÑOZ FF, GUEVARA MG, DALEO GR
Lugar:
Villa Carlos Paz, Córdoba, Argentina
Reunión:
Congreso; XLIV Reunión anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular (SAIB); 2008
Resumen:
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We have reported the
antimicrobial activity of a domain present in potato aspartic proteases, called
plant-specific insert (StAsp-PSI). This domain has a high structural
homology with Saposin-like proteins (SAPLIPs) with antimicrobial/antitumoral
activities. The aim of this work was to analyse if similarities/differences between
StAsp-PSIr and SAPLIPs, found in the cytotoxic activities, can be
explained by similar/different 3-D structures. Comparisons of NK-Lysin,
Granulysin and SP-B with StAsp-PSIr model showed that antibacterial
activity towards E. coli and B. cereus would be dependent on the
helix 1-helix 5 structure; while the hydrolytic activity towards S. aureus,
only present in SP-B and StAsp-PSIr, would be influenced by residues
L97, C98 and A100 in the helix 4 which are similar to SP-B. In addition, we
have identified residues in the helix 4 (K113, K118, K120) that may account for
the antimicrobial activity against Gram- bacteria, as reported for SP-B. The
motive of SP-B which is responsible for bacterial aggregation showed that
helices 4 and 5 would be related with this activity previously reported for StAPs.
The analysis performed here suggests that SIMILARITIES AND DIFFERENCES IN THE
STRUCTURAL FEATURES BETWEEN StAsp-PSIr AND SAPLIPs COULD EXPLAIN
CYTOTOXIC SELECTIVITY. However, mutagenesis assays will be necessary to
corroborate this hypothesis.